3DAC

Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain

Summary for 3DAC

• Entry DOI: 10.2210/pdb3dac/pdb
• Related: 1YCR 2Z5S 2Z5T 3DAB
• Descriptor: Mdm4 protein, Cellular tumor antigen p53 (3 entities in total)
• Functional Keywords: mdmx, mdm4, hdmx, hdm4, mdm-4, mdm-x, mdm2, hdm2, p53, tumor, nucleus, oncogene, apoptosis, cell cycle, disease mutation, dna-binding, transcription
• Biological source: Danio rerio (Zebrafish); More
• Total number of polymer chains: 4
• Total formula weight: 34346.86

Authors

Popowicz, G.M.,Czarna, A.,Holak, T.A. (deposition date: 2008-05-29, release date: 2008-09-02, Last modification date: 2023-11-01)

Primary citation

Popowicz, G.M.,Czarna, A.,Holak, T.A.
Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain.
Cell Cycle, 7:2441-2443, 2008

PubMed Abstract: The Mdmx oncoprotein has only recently emerged as a critical-independent to Mdm2-regulator of p53 activation. We have determined the crystal structure of the N-terminal domain of human Mdmx bound to a 15-residue transactivation domain peptide of human p53. The structure shows why antagonists of the Mdm2 binding to p53 are ineffective in the Mdmx-p53 interaction.

PubMed: 18677113
DOI: 10.4161/cc.6365

Experimental method

X-RAY DIFFRACTION (1.8 Å)